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Related Experiment Videos

Heavy-chain binding protein recognizes aberrant polypeptides translocated in vitro.

C K Kassenbrock1, P D Garcia, P Walter

  • 1Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.

Nature
|May 5, 1988
PubMed
Summary

Immunoglobulin heavy-chain binding protein (BiP) binds to misfolded or improperly glycosylated proteins in the endoplasmic reticulum. This binding occurs with completed protein chains, not those still being synthesized.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Protein Folding

Background:

  • Immunoglobulin heavy-chain binding protein (BiP) is an endoplasmic reticulum (ER) chaperone.
  • BiP is known to associate with newly synthesized proteins.
  • Its proposed functions include preventing secretion of misfolded proteins and promoting proper folding.

Purpose of the Study:

  • To investigate the specific interactions of BiP with newly synthesized polypeptides in vitro.
  • To determine the binding preferences of BiP regarding protein folding status and glycosylation.

Main Methods:

  • Utilized an in vitro protein translation-translocation system.
  • Examined the association of BiP with nonglycosylated yeast invertase and disulphide-bonded prolactin.
  • Assessed binding to both correctly and incorrectly folded/glycosylated proteins, as well as nascent vs. completed chains.

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Main Results:

  • BiP formed tight complexes with nonglycosylated yeast invertase and incorrectly disulphide-bonded prolactin.
  • BiP did not detectably associate with glycosylated invertase or correctly disulphide-bonded prolactin.
  • BiP binding was observed only with completed prolactin chains, not with chains undergoing synthesis.

Conclusions:

  • BiP exhibits high-affinity binding in vitro to aberrantly folded or glycosylated polypeptides.
  • BiP does not bind to all nascent polypeptide chains during the folding process.
  • BiP acts as a specific sensor for protein folding errors within the ER.